3BP5_RAT
ID 3BP5_RAT Reviewed; 457 AA.
AC Q91Y80;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=SH3 domain-binding protein 5;
DE Short=SH3BP-5;
DE AltName: Full=Vascular endothelial cell-specific protein 18;
GN Name=Sh3bp5; Synonyms=Sab, Vesp18;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Aoki T., Toyoda H., Nishimoto S., Tawara J., Komurasaki T.;
RT "Identification of VESP18, a vascular endothelial cell specific protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH MAPK9 AND MAPK12, PHOSPHORYLATION AT SER-353 AND SER-423,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-353 AND SER-423.
RX PubMed=15158451; DOI=10.1016/j.bbrc.2004.04.148;
RA Court N.W., Kuo I., Quigley O., Bogoyevitch M.A.;
RT "Phosphorylation of the mitochondrial protein Sab by stress-activated
RT protein kinase 3.";
RL Biochem. Biophys. Res. Commun. 319:130-137(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Functions as guanine nucleotide exchange factor (GEF) with
CC specificity for RAB11A and RAB25. Inhibits the auto- and
CC transphosphorylation activity of BTK. Plays a negative regulatory role
CC in BTK-related cytoplasmic signaling in B-cells. May be involved in
CC BCR-induced apoptotic cell death. {ECO:0000250|UniProtKB:O60239}.
CC -!- SUBUNIT: Interacts with BTK (PubMed:15158451). Interacts with all
CC isoforms of MAPK8, MAPK9, MAPK10 and MAPK12 (PubMed:15158451).
CC Interacts with GDP-bound and nucleotide-free forms of RAB11A (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z131,
CC ECO:0000269|PubMed:15158451}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:O60239}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O60239}. Mitochondrion
CC {ECO:0000269|PubMed:15158451}. Note=Colocalizes with RAB11A on
CC cytoplasmic vesicle membranes. {ECO:0000250|UniProtKB:O60239}.
CC -!- DOMAIN: The N-terminal half of the protein mediates interaction with
CC RAB11A and functions as guanine nucleotide exchange factor. Four long
CC alpha-helices (interrupted by a central kink) assemble into coiled
CC coils, giving rise to a 'V' shape. {ECO:0000250|UniProtKB:O60239}.
CC -!- SIMILARITY: Belongs to the SH3BP5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB47152.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB027562; BAB47152.1; ALT_INIT; mRNA.
DR RefSeq; NP_446463.2; NM_054011.1.
DR AlphaFoldDB; Q91Y80; -.
DR SMR; Q91Y80; -.
DR STRING; 10116.ENSRNOP00000026389; -.
DR iPTMnet; Q91Y80; -.
DR PhosphoSitePlus; Q91Y80; -.
DR PaxDb; Q91Y80; -.
DR PRIDE; Q91Y80; -.
DR GeneID; 117186; -.
DR KEGG; rno:117186; -.
DR UCSC; RGD:620220; rat.
DR CTD; 9467; -.
DR RGD; 620220; Sh3bp5.
DR VEuPathDB; HostDB:ENSRNOG00000052391; -.
DR eggNOG; KOG2008; Eukaryota.
DR HOGENOM; CLU_048895_1_0_1; -.
DR InParanoid; Q91Y80; -.
DR OMA; QFPPATR; -.
DR OrthoDB; 566222at2759; -.
DR PhylomeDB; Q91Y80; -.
DR TreeFam; TF105573; -.
DR PRO; PR:Q91Y80; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000052391; Expressed in heart and 20 other tissues.
DR Genevisible; Q91Y80; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; TAS:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0007254; P:JNK cascade; NAS:RGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IBA:GO_Central.
DR InterPro; IPR007940; SH3BP5.
DR PANTHER; PTHR19423; PTHR19423; 2.
DR Pfam; PF05276; SH3BP5; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Guanine-nucleotide releasing factor;
KW Membrane; Mitochondrion; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..457
FT /note="SH3 domain-binding protein 5"
FT /id="PRO_0000064370"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..267
FT /note="Sufficient for interaction with RAB11A and for
FT guanine nucleotide exchange activity"
FT /evidence="ECO:0000250|UniProtKB:O60239"
FT REGION 308..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..92
FT /evidence="ECO:0000250|UniProtKB:O60239"
FT COILED 99..147
FT /evidence="ECO:0000250|UniProtKB:O60239"
FT COILED 156..202
FT /evidence="ECO:0000250|UniProtKB:O60239"
FT COILED 213..257
FT /evidence="ECO:0000250|UniProtKB:O60239"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Phosphoserine; by MAPK12 and MAPK9"
FT /evidence="ECO:0000269|PubMed:15158451"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z131"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z131"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 423
FT /note="Phosphoserine; by MAPK12"
FT /evidence="ECO:0000269|PubMed:15158451,
FT ECO:0007744|PubMed:22673903"
FT MUTAGEN 353
FT /note="S->A: Large decrease in phosphorylation by SAPK3."
FT /evidence="ECO:0000269|PubMed:15158451"
FT MUTAGEN 423
FT /note="S->A: Slight decrease in phosphorylation by SAPK3."
FT /evidence="ECO:0000269|PubMed:15158451"
SQ SEQUENCE 457 AA; 50829 MW; 68339F6993950B7C CRC64;
MDTALKRSRS EEPVELPPPA REAEEKEEEE ERMEQGLEEE EEVDPRIQGE LEKLNQSTDD
INRRETELED ARQKFRSVLV EATVKLDELA KKIGKAVEDS KPYWEARRVA RQAQLEAQKA
TQDFQRATEV LRAAKETISL AEQRLLEDDK RQFDSAWQEM LNHATQRVME AEQTKTRSEL
VHKETAARYN AAMGRMRQLE KKLKRAINKS KPYFELKAKY YVQLEQLKKT VDDLQAKLAL
AKGEYKAALK SLERISDEIH ERRRSNAMGP RGCGVGAEGS ITSVENLPAS KPEPDAISVA
SEAFEDDNCG NLVSEDDSET QSVSSFSSGP TSPSEMPDQF PAVARPGSLD LPSPVSLSEF
GMMFPILGPR SECSGASSPE CEVERGDRAE GAENKMSDKA NNNRVLSSTS AGGGRSRSQS
STSLEGQALE TRMKQLSLQC SKGREGIIAD IKTVQIG
